SV2B_MOUSE
ID SV2B_MOUSE Reviewed; 683 AA.
AC Q8BG39; Q80TT1; Q9ES95;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Synaptic vesicle glycoprotein 2B;
DE Short=Synaptic vesicle protein 2B;
GN Name=Sv2b; Synonyms=Kiaa0735;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Corpora quadrigemina, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=129/Sv;
RX PubMed=10624962; DOI=10.1016/s0896-6273(00)81046-6;
RA Janz R., Goda Y., Geppert M., Missler M., Suedhof T.C.;
RT "SV2A and SV2B function as redundant Ca2+ regulators in neurotransmitter
RT release.";
RL Neuron 24:1003-1016(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-683.
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10611374; DOI=10.1073/pnas.96.26.15268;
RA Crowder K.M., Gunther J.M., Jones T.A., Hale B.D., Zhang H.Z.,
RA Peterson M.R., Scheller R.H., Chavkin C., Bajjalieh S.M.;
RT "Abnormal neurotransmission in mice lacking synaptic vesicle protein 2A
RT (SV2A).";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15268-15273(1999).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12687700; DOI=10.1002/cne.10636;
RA Wang M.M., Janz R., Belizaire R., Frishman L.J., Sherry D.M.;
RT "Differential distribution and developmental expression of synaptic vesicle
RT protein 2 isoforms in the mouse retina.";
RL J. Comp. Neurol. 460:106-122(2003).
RN [7]
RP INTERACTION WITH SYT1; SYNTAXIN-1 AND SNAP25.
RX PubMed=15466855; DOI=10.1074/jbc.m407502200;
RA Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.;
RT "SV2B regulates synaptotagmin 1 by direct interaction.";
RL J. Biol. Chem. 279:52124-52131(2004).
RN [8]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE A RECEPTOR (MICROBIAL INFECTION),
RP SUBUNIT (MICROBIAL INFECTION), TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16543415; DOI=10.1126/science.1123654;
RA Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R., Chapman E.R.;
RT "SV2 is the protein receptor for botulinum neurotoxin A.";
RL Science 312:592-596(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE E RECEPTOR (MICROBIAL INFECTION),
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18815274; DOI=10.1091/mbc.e08-07-0765;
RA Dong M., Liu H., Tepp W.H., Johnson E.A., Janz R., Chapman E.R.;
RT "Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E
RT into neurons.";
RL Mol. Biol. Cell 19:5226-5237(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND THR-36, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP POSSIBLE FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE D RECEPTOR (MICROBIAL
RP INFECTION), AND DISRUPTION PHENOTYPE.
RX PubMed=21483489; DOI=10.1371/journal.ppat.1002008;
RA Peng L., Tepp W.H., Johnson E.A., Dong M.;
RT "Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides
RT as receptors.";
RL PLoS Pathog. 7:E1002008-E1002008(2011).
RN [13]
RP NOT RECEPTOR FOR C.BOTULINUM NEUROTOXIN TYPE D (MICROBIAL INFECTION).
RX PubMed=21632541; DOI=10.1074/jbc.m111.254086;
RA Kroken A.R., Karalewitz A.P., Fu Z., Kim J.J., Barbieri J.T.;
RT "Novel ganglioside-mediated entry of botulinum neurotoxin serotype D into
RT neurons.";
RL J. Biol. Chem. 286:26828-26837(2011).
CC -!- FUNCTION: Probably plays a role in the control of regulated secretion
CC in neural and endocrine cells. {ECO:0000305|PubMed:10624962}.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type A (BoNT/A, botA); the toxin probably binds via extracellular loop
CC 4 (PubMed:16543415). {ECO:0000269|PubMed:16543415}.
CC -!- FUNCTION: (Microbial infection) Possible receptor for C.botulinum
CC neurotoxin type D (BoNT/D, botD) (PubMed:21483489). Not a receptor for
CC C.botulinum neurotoxin type D (BoNT/D, botD) (PubMed:21632541).
CC {ECO:0000269|PubMed:21632541}.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type E (BoNT/E); the toxin probably binds via extracellular loop 4
CC (PubMed:18815274). It probably requires glycosylation of Asn-516
CC (PubMed:18815274). {ECO:0000269|PubMed:18815274,
CC ECO:0000305|PubMed:18815274}.
CC -!- SUBUNIT: Interacts with SYT1 in a calcium-independent manner. Forms a
CC complex with SYT1, syntaxin-1 and SNAP25.
CC {ECO:0000269|PubMed:15466855}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type A (BoNT/A, botA). {ECO:0000269|PubMed:18815274,
CC ECO:0000305|PubMed:16543415}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type D (BoNT/D, botD) (PubMed:21483489). No evidence for its
CC interaction with BoNT/D has also been published (PubMed:21632541).
CC {ECO:0000269|PubMed:21483489, ECO:0000269|PubMed:21632541}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q63564}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000250|UniProtKB:Q63564}. Note=Associated with synaptic-like
CC microvesicles but not with insulin-containing vesicles in insulin-
CC secreting cells of the pancreas (By similarity). Localizes to
CC microvesicles in the pinealocytes. Localizes to the acrosome in
CC spermatids (By similarity). {ECO:0000250|UniProtKB:Q63564}.
CC -!- TISSUE SPECIFICITY: Expressed in ribbon synapses of the retina (at
CC protein level) (PubMed:12687700). Expressed in diaphragm motor nerve
CC terminals (at protein level) (PubMed:16543415). Expressed in
CC hippocampus neurons (at protein level) (PubMed:18815274).
CC {ECO:0000269|PubMed:12687700, ECO:0000269|PubMed:16543415,
CC ECO:0000269|PubMed:18815274}.
CC -!- DEVELOPMENTAL STAGE: Expressed during synaptogenesis in the retina (at
CC protein level). {ECO:0000269|PubMed:12687700}.
CC -!- INDUCTION: Up-regulated upon Sv2a depletion.
CC {ECO:0000269|PubMed:10611374}.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:18815274}.
CC -!- PTM: The N-terminal cytoplasmic domain is phosphorylated by CK1.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice display no particular phenotype
CC (PubMed:10624962). Single knockout mice survive significantly longer
CC than wild-type mice upon exposure to C.botulinum neurotoxin type A
CC (BoNT/A, botA) (PubMed:16543415). Mice lacking both Sv2a and Sv2b
CC experience severe epileptic seizures and die immediately or shortly
CC after birth similarly to mice lacking only Sv2a (PubMed:10624962).
CC Single knockout mice bind reduced amounts of BoNT/A than wild-type mice
CC (PubMed:16543415). Single knockout mice are significantly more
CC resistant to C.botulinum neurotoxin type E (BoNT/E) than wild-type mice
CC (PubMed:18815274). In single knockout mice, synaptobrevin (VAMP, the
CC target of C.botulinum neurotoxin type D, BoNT/D) is degraded by BoNT/D,
CC and hippocampal neurons bind BoNT/D (PubMed:21483489). Hippocampal
CC neurons from young mice lacking both Sv2a and Sv2b do not bind BoNT/A,
CC nor do they take it up (PubMed:16543415, PubMed:18815274). Hippocampal
CC neurons from young mice lacking both Sv2a and Sv2b do not bind
CC C.botulinum neurotoxin type E (BoNT/E), nor do they take it up
CC (PubMed:18815274). Hippocampal neurons from young mice lacking both
CC Sv2a and Sv2b do not bind C.botulinum neurotoxin type D (BoNT/D, botD),
CC nor do they take it up (PubMed:21483489). Hippocampal neurons from
CC young mice lacking both Sv2a and Sv2b take up C.botulinum neurotoxin
CC type C (BoNT/C) and C.botulinum neurotoxin type F (BonT/F, botF)
CC normally (PubMed:21483489). {ECO:0000269|PubMed:10611374,
CC ECO:0000269|PubMed:10624962, ECO:0000269|PubMed:16543415,
CC ECO:0000269|PubMed:18815274, ECO:0000269|PubMed:21483489}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC -!- CAUTION: The use of this protein as a coreceptor for C.botulinum type D
CC (BoNT/D, botD) is controversial. In double SV2A/SV2B knockout mice
CC BoNT/D does not degrade its synaptobrevin target; introducing SV2A,
CC SV2B or SV2C restores target cleavage (PubMed:21483489). However
CC another group does not find a convincing interaction with SV2
CC (PubMed:21632541). {ECO:0000269|PubMed:21483489,
CC ECO:0000269|PubMed:21632541}.
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DR EMBL; AK029736; BAC26590.1; -; mRNA.
DR EMBL; AK043830; BAC31669.1; -; mRNA.
DR EMBL; AK139478; BAE24029.1; -; mRNA.
DR EMBL; AK140104; BAE24238.1; -; mRNA.
DR EMBL; AK147261; BAE27804.1; -; mRNA.
DR EMBL; BC060224; AAH60224.1; -; mRNA.
DR EMBL; AF196782; AAG28491.1; -; Genomic_DNA.
DR EMBL; AK122359; BAC65641.1; -; mRNA.
DR CCDS; CCDS21368.1; -.
DR RefSeq; NP_001103223.1; NM_001109753.1.
DR RefSeq; NP_705807.2; NM_153579.4.
DR RefSeq; XP_006541122.1; XM_006541059.3.
DR RefSeq; XP_006541123.1; XM_006541060.3.
DR RefSeq; XP_006541124.1; XM_006541061.2.
DR RefSeq; XP_017167699.1; XM_017312210.1.
DR RefSeq; XP_017167701.1; XM_017312212.1.
DR AlphaFoldDB; Q8BG39; -.
DR BioGRID; 211036; 4.
DR IntAct; Q8BG39; 1.
DR MINT; Q8BG39; -.
DR STRING; 10090.ENSMUSP00000127245; -.
DR GlyGen; Q8BG39; 3 sites.
DR iPTMnet; Q8BG39; -.
DR PhosphoSitePlus; Q8BG39; -.
DR SwissPalm; Q8BG39; -.
DR MaxQB; Q8BG39; -.
DR PaxDb; Q8BG39; -.
DR PeptideAtlas; Q8BG39; -.
DR PRIDE; Q8BG39; -.
DR ProteomicsDB; 258676; -.
DR Antibodypedia; 29003; 149 antibodies from 26 providers.
DR DNASU; 64176; -.
DR Ensembl; ENSMUST00000085164; ENSMUSP00000082254; ENSMUSG00000053025.
DR Ensembl; ENSMUST00000165175; ENSMUSP00000127245; ENSMUSG00000053025.
DR Ensembl; ENSMUST00000206344; ENSMUSP00000146049; ENSMUSG00000053025.
DR GeneID; 64176; -.
DR KEGG; mmu:64176; -.
DR UCSC; uc009hwk.2; mouse.
DR CTD; 9899; -.
DR MGI; MGI:1927338; Sv2b.
DR VEuPathDB; HostDB:ENSMUSG00000053025; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00950000182940; -.
DR HOGENOM; CLU_001265_46_15_1; -.
DR InParanoid; Q8BG39; -.
DR OMA; TNQVSDD; -.
DR OrthoDB; 724235at2759; -.
DR PhylomeDB; Q8BG39; -.
DR TreeFam; TF324824; -.
DR BioGRID-ORCS; 64176; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Sv2b; mouse.
DR PRO; PR:Q8BG39; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BG39; protein.
DR Bgee; ENSMUSG00000053025; Expressed in subiculum and 171 other tissues.
DR ExpressionAtlas; Q8BG39; baseline and differential.
DR Genevisible; Q8BG39; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:MGI.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR InterPro; IPR022308; SV2.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR01299; synapt_SV2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Glycoprotein; Membrane; Neurotransmitter transport;
KW Phosphoprotein; Receptor; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..683
FT /note="Synaptic vesicle glycoprotein 2B"
FT /id="PRO_0000239769"
FT TOPO_DOM 1..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..535
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..592
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 650..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 423
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 18
FT /note="G -> D (in Ref. 3; AAG28491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 77457 MW; CBDC19B281B9E4F3 CRC64;
MDDYRYRDNY EGYAPSDGYY RSNEQNQEED AQSDVTEGHD EEDEIYEGEY QGIPHPDDVK
SKQTKMAPSR ADGLGGQADL MAERMEDEEE LAHQYETIID ECGHGRFQWT LFFVLGLALM
ADGVEIFVVS FALPSAEKDM CLSSSKKGML GLIVYLGMMA GAFILGGLAD KLGRKKVLSM
SLAINASFAS LSSFVQGYGA FLFCRLISGI GIGGSLPIVF AYFSEFLSRE KRGEHLSWLG
IFWMTGGIYA SAMAWSIIPH YGWGFSMGTN YHFHSWRVFV IVCALPATVS MVALKFMPES
PRFLLEMGKH DEAWMILKQV HDTNMRAKGT PEKVFTVSHI KTPKQMDEFI EIQSSTGTWY
QRWLVRFMTI FKQVWDNALY CVMGPYRMNT LILAVVWFTM ALSYYGLTVW FPDMIRYFQD
EEYKSKMKVF FGEHVHGATI NFTMENQIHQ HGKLVNDKFI KMYFKHVLFE DTFFDKCYFE
DVTSTDTYFK NCTIESTTFY NTDLYKHKFI NCRFINSTFL EQKEGCHMDF EEDNDFLIYL
VSFLGSLSVL PGNIISALLM DRIGRLKMIG GSMLISAVCC FFLFFGNSES AMIGWQCLFC
GTSIAAWNAL DVITVELYPT NQRATAFGIL NGLCKFGAIL GNTIFASFVG ITKVVPILLA
AASLVGGGLI ALRLPETREQ VLM
